| content |
HEADER HYDROLASE 03-MAY-17 5VOL
TITLE BACINT_04212 FERULIC ACID ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: UNP RESIDUES 21-294;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES INTESTINALIS DSM 17393;
SOURCE 3 ORGANISM_TAXID: 471870;
SOURCE 4 GENE: BACINT_04212;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS FERULIC ACID ESTERASE, BACTEROIDES INTESTINALIS, ARABINOXYLAN
KEYWDS 2 ESTERASE, CARBOHYDRATE ESTERASE FAMILY 1, CE1, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.M.KOROPATKIN,I.CANN,R.I.MACKIE
REVDAT 1 19-JUL-17 5VOL 0
JRNL AUTH D.WEFERS,J.J.V.CAVALCANTE,R.R.SCHENDEL,J.DEVERYSHETTY,
JRNL AUTH 2 K.WANG,Z.WAWRZAK,R.I.MACKIE,N.M.KOROPATKIN,I.CANN
JRNL TITL BIOCHEMICAL AND STRUCTURAL ANALYSES OF TWO CRYPTIC ESTERASES
JRNL TITL 2 IN BACTEROIDES INTESTINALIS AND THEIR SYNERGISTIC ACTIVITIES
JRNL TITL 3 WITH COGNATE XYLANASES.
JRNL REF J. MOL. BIOL. 2017
JRNL REFN ESSN 1089-8638
JRNL PMID 28669823
JRNL DOI 10.1016/J.JMB.2017.06.017
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 207681
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 10450
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 56.6720 - 6.1498 0.97 6800 373 0.1384 0.1453
REMARK 3 2 6.1498 - 4.8821 0.99 6635 377 0.1363 0.1661
REMARK 3 3 4.8821 - 4.2652 0.99 6698 309 0.1216 0.1339
REMARK 3 4 4.2652 - 3.8754 0.99 6592 351 0.1290 0.1472
REMARK 3 5 3.8754 - 3.5976 0.99 6622 336 0.1443 0.1671
REMARK 3 6 3.5976 - 3.3856 0.99 6626 322 0.1522 0.1855
REMARK 3 7 3.3856 - 3.2160 0.99 6573 355 0.1640 0.1921
REMARK 3 8 3.2160 - 3.0760 1.00 6645 329 0.1714 0.2103
REMARK 3 9 3.0760 - 2.9576 1.00 6539 345 0.1740 0.2011
REMARK 3 10 2.9576 - 2.8556 1.00 6567 364 0.1751 0.2058
REMARK 3 11 2.8556 - 2.7663 1.00 6600 336 0.1699 0.2093
REMARK 3 12 2.7663 - 2.6872 1.00 6560 358 0.1759 0.2050
REMARK 3 13 2.6872 - 2.6165 1.00 6523 342 0.1830 0.2330
REMARK 3 14 2.6165 - 2.5526 1.00 6606 328 0.1798 0.2053
REMARK 3 15 2.5526 - 2.4946 1.00 6582 334 0.1843 0.2331
REMARK 3 16 2.4946 - 2.4415 1.00 6607 311 0.1897 0.2385
REMARK 3 17 2.4415 - 2.3927 1.00 6529 353 0.1878 0.2324
REMARK 3 18 2.3927 - 2.3475 1.00 6587 340 0.1867 0.2289
REMARK 3 19 2.3475 - 2.3056 1.00 6490 386 0.1866 0.2281
REMARK 3 20 2.3056 - 2.2665 1.00 6552 351 0.1976 0.2352
REMARK 3 21 2.2665 - 2.2300 1.00 6537 357 0.2018 0.2588
REMARK 3 22 2.2300 - 2.1957 1.00 6529 353 0.2069 0.2485
REMARK 3 23 2.1957 - 2.1634 1.00 6563 355 0.2031 0.2540
REMARK 3 24 2.1634 - 2.1329 1.00 6529 343 0.2106 0.2363
REMARK 3 25 2.1329 - 2.1041 1.00 6528 347 0.2248 0.2770
REMARK 3 26 2.1041 - 2.0767 1.00 6544 348 0.2328 0.2588
REMARK 3 27 2.0767 - 2.0508 1.00 6498 357 0.2401 0.2699
REMARK 3 28 2.0508 - 2.0261 1.00 6507 355 0.2400 0.2820
REMARK 3 29 2.0261 - 2.0025 1.00 6517 369 0.2502 0.2819
REMARK 3 30 2.0025 - 1.9800 1.00 6546 366 0.2656 0.2986
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 17540
REMARK 3 ANGLE : 0.986 23720
REMARK 3 CHIRALITY : 0.042 2425
REMARK 3 PLANARITY : 0.005 3050
REMARK 3 DIHEDRAL : 12.696 6330
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5VOL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1000227773.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 207704
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 56.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.07951
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.7700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.74540
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.440
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: IN-HOUSE SAD MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES SODIUM PH 7.5, 10 % V/V 2
REMARK 280 -PROPANOL, 20 % W/V POLYETHYLENE GLYCOL 4000, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 63.96000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.29500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.89500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 86.29500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 63.96000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.89500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LYS A 14
REMARK 465 GLN A 15
REMARK 465 ASN A 16
REMARK 465 ALA A 17
REMARK 465 PRO A 18
REMARK 465 TRP A 19
REMARK 465 GLN A 184
REMARK 465 GLY A 185
REMARK 465 ALA A 186
REMARK 465 VAL A 187
REMARK 465 PRO A 188
REMARK 465 ALA A 189
REMARK 465 ASP A 190
REMARK 465 LYS A 287
REMARK 465 GLU A 288
REMARK 465 LYS B 14
REMARK 465 GLN B 15
REMARK 465 ASN B 16
REMARK 465 ALA B 17
REMARK 465 PRO B 18
REMARK 465 TRP B 19
REMARK 465 GLY B 185
REMARK 465 ALA B 186
REMARK 465 VAL B 187
REMARK 465 LYS B 287
REMARK 465 GLU B 288
REMARK 465 LYS C 14
REMARK 465 GLN C 15
REMARK 465 ASN C 16
REMARK 465 ALA C 17
REMARK 465 GLY C 286
REMARK 465 LYS C 287
REMARK 465 GLU C 288
REMARK 465 LYS D 14
REMARK 465 GLN D 15
REMARK 465 ASN D 16
REMARK 465 ALA D 17
REMARK 465 PRO D 18
REMARK 465 TRP D 19
REMARK 465 ALA D 186
REMARK 465 VAL D 187
REMARK 465 GLY D 286
REMARK 465 LYS D 287
REMARK 465 GLU D 288
REMARK 465 LYS E 14
REMARK 465 GLN E 15
REMARK 465 ASN E 16
REMARK 465 ALA E 17
REMARK 465 PRO E 18
REMARK 465 GLN E 184
REMARK 465 GLY E 185
REMARK 465 ALA E 186
REMARK 465 GLY E 286
REMARK 465 LYS E 287
REMARK 465 GLU E 288
REMARK 465 LYS F 14
REMARK 465 GLN F 15
REMARK 465 ASN F 16
REMARK 465 ALA F 17
REMARK 465 PRO F 18
REMARK 465 TRP F 19
REMARK 465 GLN F 184
REMARK 465 GLY F 185
REMARK 465 ALA F 186
REMARK 465 VAL F 187
REMARK 465 PRO F 188
REMARK 465 ALA F 189
REMARK 465 ASP F 190
REMARK 465 LYS F 287
REMARK 465 GLU F 288
REMARK 465 LYS G 14
REMARK 465 GLN G 15
REMARK 465 ASN G 16
REMARK 465 ALA G 17
REMARK 465 PRO G 18
REMARK 465 TRP G 19
REMARK 465 GLN G 184
REMARK 465 GLY G 185
REMARK 465 ALA G 186
REMARK 465 VAL G 187
REMARK 465 PRO G 188
REMARK 465 ALA G 189
REMARK 465 ASP G 190
REMARK 465 ASP G 191
REMARK 465 GLY G 286
REMARK 465 LYS G 287
REMARK 465 GLU G 288
REMARK 465 LYS H 14
REMARK 465 GLN H 15
REMARK 465 ASN H 16
REMARK 465 ALA H 17
REMARK 465 PRO H 18
REMARK 465 TRP H 19
REMARK 465 ASN H 20
REMARK 465 GLU H 183
REMARK 465 GLN H 184
REMARK 465 GLY H 185
REMARK 465 ALA H 186
REMARK 465 VAL H 187
REMARK 465 PRO H 188
REMARK 465 ALA H 189
REMARK 465 ASP H 190
REMARK 465 GLY H 286
REMARK 465 LYS H 287
REMARK 465 GLU H 288
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 411 O HOH B 560 2.13
REMARK 500 OE1 GLU B 214 O HOH B 401 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU D 151 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TRP A 67 -22.68 74.82
REMARK 500 TRP A 119 83.12 -151.84
REMARK 500 GLU A 128 -60.76 -124.54
REMARK 500 SER A 152 -118.44 54.42
REMARK 500 TRP B 67 -21.03 75.74
REMARK 500 ASN B 105 109.11 -53.97
REMARK 500 TRP B 119 89.32 -158.98
REMARK 500 GLU B 128 -52.23 -124.70
REMARK 500 SER B 152 -125.92 58.39
REMARK 500 TRP C 67 -22.04 76.92
REMARK 500 TRP C 119 84.86 -162.09
REMARK 500 GLU C 128 -54.60 -121.39
REMARK 500 SER C 152 -120.15 54.87
REMARK 500 TRP D 67 -35.14 74.68
REMARK 500 TRP D 119 88.80 -156.15
REMARK 500 SER D 152 -123.16 56.58
REMARK 500 TRP E 67 -21.22 77.39
REMARK 500 TRP E 119 89.19 -159.86
REMARK 500 SER E 152 -122.12 57.92
REMARK 500 ASP E 191 88.52 66.12
REMARK 500 TRP F 67 -27.56 81.46
REMARK 500 PRO F 117 105.94 -53.88
REMARK 500 SER F 152 -123.47 56.80
REMARK 500 TRP G 67 -21.35 80.71
REMARK 500 TRP G 119 88.81 -156.20
REMARK 500 SER G 152 -122.74 59.30
REMARK 500 TRP H 67 -25.30 78.55
REMARK 500 ALA H 102 25.16 -145.13
REMARK 500 PRO H 117 101.94 -52.31
REMARK 500 TRP H 119 89.35 -151.07
REMARK 500 GLU H 128 -56.86 -121.52
REMARK 500 SER H 152 -123.75 60.93
REMARK 500 PRO H 192 1.76 -67.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 234 OD1
REMARK 620 2 ASP A 234 OD2 51.2
REMARK 620 3 ASP A 235 OD2 76.6 112.7
REMARK 620 4 ASP A 262 OD1 87.8 111.9 104.0
REMARK 620 5 GLN B 257 OE1 126.0 84.4 157.1 81.9
REMARK 620 6 HOH A 554 O 143.1 160.9 70.5 84.4 88.5
REMARK 620 7 HOH A 418 O 104.1 74.3 82.5 167.5 88.1 87.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 257 OE1
REMARK 620 2 ASP B 234 OD1 127.4
REMARK 620 3 ASP B 234 OD2 84.7 51.3
REMARK 620 4 ASP B 235 OD2 154.5 77.8 114.4
REMARK 620 5 ASP B 262 OD1 83.6 88.8 113.0 102.6
REMARK 620 6 HOH B 428 O 88.5 104.0 76.1 80.5 167.2
REMARK 620 7 HOH B 521 O 89.3 142.2 158.5 66.7 86.6 83.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 234 OD1
REMARK 620 2 ASP C 234 OD2 52.7
REMARK 620 3 ASP C 235 OD2 73.6 113.0
REMARK 620 4 ASP C 262 OD1 90.8 113.4 103.0
REMARK 620 5 GLN F 257 OE1 127.7 83.0 158.4 82.2
REMARK 620 6 HOH C 413 O 105.2 75.2 85.1 163.6 85.2
REMARK 620 7 HOH C 544 O 141.8 162.4 72.5 80.1 88.0 89.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 257 OE1
REMARK 620 2 ASP F 234 OD1 125.2
REMARK 620 3 ASP F 234 OD2 84.1 51.4
REMARK 620 4 ASP F 235 OD2 157.2 77.5 113.1
REMARK 620 5 ASP F 262 OD1 82.7 87.6 113.5 102.4
REMARK 620 6 HOH F 503 O 89.8 142.8 159.8 68.8 84.6
REMARK 620 7 HOH F 426 O 88.9 104.0 73.5 82.4 168.2 87.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 234 OD1
REMARK 620 2 ASP D 234 OD2 49.8
REMARK 620 3 ASP D 235 OD2 73.7 112.3
REMARK 620 4 ASP D 262 OD1 86.3 109.3 99.3
REMARK 620 5 GLN E 257 OE1 122.0 81.7 164.3 81.9
REMARK 620 6 HOH D 558 O 147.6 159.3 76.3 86.9 88.2
REMARK 620 7 HOH D 451 O 107.0 75.5 92.0 164.6 84.5 85.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN D 257 OE1
REMARK 620 2 ASP E 234 OD1 125.7
REMARK 620 3 ASP E 234 OD2 81.8 51.5
REMARK 620 4 ASP E 235 OD2 154.3 79.4 116.6
REMARK 620 5 ASP E 262 OD1 82.3 89.4 110.6 105.4
REMARK 620 6 HOH E 416 O 90.3 101.7 76.4 77.9 168.9
REMARK 620 7 HOH E 522 O 88.0 145.3 157.9 68.3 87.2 84.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 234 OD1
REMARK 620 2 ASP G 234 OD2 49.9
REMARK 620 3 ASP G 235 OD2 78.6 114.1
REMARK 620 4 ASP G 262 OD1 88.2 112.9 101.4
REMARK 620 5 GLN H 257 OE1 125.6 84.8 155.7 83.7
REMARK 620 6 HOH G 440 O 105.2 74.7 85.0 166.2 85.6
REMARK 620 7 HOH G 459 O 139.5 160.2 63.3 86.5 93.6 85.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN G 257 OE1
REMARK 620 2 ASP H 234 OD1 122.5
REMARK 620 3 ASP H 234 OD2 79.8 51.0
REMARK 620 4 ASP H 235 OD2 157.1 78.2 111.9
REMARK 620 5 ASP H 262 OD1 86.7 86.5 111.9 105.7
REMARK 620 6 HOH H 423 O 85.4 110.3 81.3 77.4 163.1
REMARK 620 7 HOH G 518 O 90.6 144.9 160.7 72.1 83.9 81.3
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA D 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA D 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA F 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 301
DBREF 5VOL A 15 288 UNP B3CET1 B3CET1_9BACE 21 294
DBREF 5VOL B 15 288 UNP B3CET1 B3CET1_9BACE 21 294
DBREF 5VOL C 15 288 UNP B3CET1 B3CET1_9BACE 21 294
DBREF 5VOL D 15 288 UNP B3CET1 B3CET1_9BACE 21 294
DBREF 5VOL E 15 288 UNP B3CET1 B3CET1_9BACE 21 294
DBREF 5VOL F 15 288 UNP B3CET1 B3CET1_9BACE 21 294
DBREF 5VOL G 15 288 UNP B3CET1 B3CET1_9BACE 21 294
DBREF 5VOL H 15 288 UNP B3CET1 B3CET1_9BACE 21 294
SEQADV 5VOL LYS A 14 UNP B3CET1 EXPRESSION TAG
SEQADV 5VOL LYS B 14 UNP B3CET1 EXPRESSION TAG
SEQADV 5VOL LYS C 14 UNP B3CET1 EXPRESSION TAG
SEQADV 5VOL LYS D 14 UNP B3CET1 EXPRESSION TAG
SEQADV 5VOL LYS E 14 UNP B3CET1 EXPRESSION TAG
SEQADV 5VOL LYS F 14 UNP B3CET1 EXPRESSION TAG
SEQADV 5VOL LYS G 14 UNP B3CET1 EXPRESSION TAG
SEQADV 5VOL LYS H 14 UNP B3CET1 EXPRESSION TAG
SEQRES 1 A 275 LYS GLN ASN ALA PRO TRP ASN PHE GLN SER LYS VAL VAL
SEQRES 2 A 275 THR ASP THR LEU PHE SER LYS VAL LEU ASN SER LYS ARG
SEQRES 3 A 275 ALA TYR THR VAL PHE LEU PRO LYS SER PHE GLU GLN ASN
SEQRES 4 A 275 LYS GLU LYS LYS TYR PRO VAL LEU TYR LEU LEU HIS GLY
SEQRES 5 A 275 MET TRP GLU THR ASN PRO VAL TRP ALA GLU ARG GLY HIS
SEQRES 6 A 275 VAL LYS ASP VAL MET ASP ARG LEU VAL ALA SER GLY GLU
SEQRES 7 A 275 ALA CYS GLU MET ILE ILE VAL THR PRO ASN ALA GLY GLY
SEQRES 8 A 275 ASN ILE HIS LEU GLU TRP ASN GLY TYR PHE ASP MET PRO
SEQRES 9 A 275 GLY TRP LYS TYR GLU THR PHE PHE TYR THR GLU PHE LEU
SEQRES 10 A 275 PRO TYR ILE GLU LYS LYS TYR ARG VAL ILE GLY ASP ARG
SEQRES 11 A 275 GLN HIS ARG ALA ILE ALA GLY LEU SER MET GLY GLY GLY
SEQRES 12 A 275 GLY ALA THR ASN TYR GLY GLN ARG HIS SER ASP MET PHE
SEQRES 13 A 275 CYS ALA VAL TYR ALA MET SER ALA LEU MET SER ILE PRO
SEQRES 14 A 275 GLU GLN GLY ALA VAL PRO ALA ASP ASP PRO ASN SER LYS
SEQRES 15 A 275 ILE ALA ILE LEU THR ARG SER VAL ILE GLU ASN SER CYS
SEQRES 16 A 275 VAL LYS TYR VAL MET GLU ALA ASP GLU ASP ARG LYS ALA
SEQRES 17 A 275 ASP LEU ARG SER VAL ALA TRP PHE VAL ASP CYS GLY ASP
SEQRES 18 A 275 ASP ASP PHE LEU LEU ASP ARG ASN ILE GLU PHE TYR GLN
SEQRES 19 A 275 ALA MET ARG ASN ALA GLY VAL PRO CYS GLN PHE ARG VAL
SEQRES 20 A 275 ARG ASP GLY GLY HIS ASP TRP GLU TYR TRP HIS SER ALA
SEQRES 21 A 275 LEU TYR GLN CYS LEU PRO PHE VAL THR ARG ILE PHE GLY
SEQRES 22 A 275 LYS GLU
SEQRES 1 B 275 LYS GLN ASN ALA PRO TRP ASN PHE GLN SER LYS VAL VAL
SEQRES 2 B 275 THR ASP THR LEU PHE SER LYS VAL LEU ASN SER LYS ARG
SEQRES 3 B 275 ALA TYR THR VAL PHE LEU PRO LYS SER PHE GLU GLN ASN
SEQRES 4 B 275 LYS GLU LYS LYS TYR PRO VAL LEU TYR LEU LEU HIS GLY
SEQRES 5 B 275 MET TRP GLU THR ASN PRO VAL TRP ALA GLU ARG GLY HIS
SEQRES 6 B 275 VAL LYS ASP VAL MET ASP ARG LEU VAL ALA SER GLY GLU
SEQRES 7 B 275 ALA CYS GLU MET ILE ILE VAL THR PRO ASN ALA GLY GLY
SEQRES 8 B 275 ASN ILE HIS LEU GLU TRP ASN GLY TYR PHE ASP MET PRO
SEQRES 9 B 275 GLY TRP LYS TYR GLU THR PHE PHE TYR THR GLU PHE LEU
SEQRES 10 B 275 PRO TYR ILE GLU LYS LYS TYR ARG VAL ILE GLY ASP ARG
SEQRES 11 B 275 GLN HIS ARG ALA ILE ALA GLY LEU SER MET GLY GLY GLY
SEQRES 12 B 275 GLY ALA THR ASN TYR GLY GLN ARG HIS SER ASP MET PHE
SEQRES 13 B 275 CYS ALA VAL TYR ALA MET SER ALA LEU MET SER ILE PRO
SEQRES 14 B 275 GLU GLN GLY ALA VAL PRO ALA ASP ASP PRO ASN SER LYS
SEQRES 15 B 275 ILE ALA ILE LEU THR ARG SER VAL ILE GLU ASN SER CYS
SEQRES 16 B 275 VAL LYS TYR VAL MET GLU ALA ASP GLU ASP ARG LYS ALA
SEQRES 17 B 275 ASP LEU ARG SER VAL ALA TRP PHE VAL ASP CYS GLY ASP
SEQRES 18 B 275 ASP ASP PHE LEU LEU ASP ARG ASN ILE GLU PHE TYR GLN
SEQRES 19 B 275 ALA MET ARG ASN ALA GLY VAL PRO CYS GLN PHE ARG VAL
SEQRES 20 B 275 ARG ASP GLY GLY HIS ASP TRP GLU TYR TRP HIS SER ALA
SEQRES 21 B 275 LEU TYR GLN CYS LEU PRO PHE VAL THR ARG ILE PHE GLY
SEQRES 22 B 275 LYS GLU
SEQRES 1 C 275 LYS GLN ASN ALA PRO TRP ASN PHE GLN SER LYS VAL VAL
SEQRES 2 C 275 THR ASP THR LEU PHE SER LYS VAL LEU ASN SER LYS ARG
SEQRES 3 C 275 ALA TYR THR VAL PHE LEU PRO LYS SER PHE GLU GLN ASN
SEQRES 4 C 275 LYS GLU LYS LYS TYR PRO VAL LEU TYR LEU LEU HIS GLY
SEQRES 5 C 275 MET TRP GLU THR ASN PRO VAL TRP ALA GLU ARG GLY HIS
SEQRES 6 C 275 VAL LYS ASP VAL MET ASP ARG LEU VAL ALA SER GLY GLU
SEQRES 7 C 275 ALA CYS GLU MET ILE ILE VAL THR PRO ASN ALA GLY GLY
SEQRES 8 C 275 ASN ILE HIS LEU GLU TRP ASN GLY TYR PHE ASP MET PRO
SEQRES 9 C 275 GLY TRP LYS TYR GLU THR PHE PHE TYR THR GLU PHE LEU
SEQRES 10 C 275 PRO TYR ILE GLU LYS LYS TYR ARG VAL ILE GLY ASP ARG
SEQRES 11 C 275 GLN HIS ARG ALA ILE ALA GLY LEU SER MET GLY GLY GLY
SEQRES 12 C 275 GLY ALA THR ASN TYR GLY GLN ARG HIS SER ASP MET PHE
SEQRES 13 C 275 CYS ALA VAL TYR ALA MET SER ALA LEU MET SER ILE PRO
SEQRES 14 C 275 GLU GLN GLY ALA VAL PRO ALA ASP ASP PRO ASN SER LYS
SEQRES 15 C 275 ILE ALA ILE LEU THR ARG SER VAL ILE GLU ASN SER CYS
SEQRES 16 C 275 VAL LYS TYR VAL MET GLU ALA ASP GLU ASP ARG LYS ALA
SEQRES 17 C 275 ASP LEU ARG SER VAL ALA TRP PHE VAL ASP CYS GLY ASP
SEQRES 18 C 275 ASP ASP PHE LEU LEU ASP ARG ASN ILE GLU PHE TYR GLN
SEQRES 19 C 275 ALA MET ARG ASN ALA GLY VAL PRO CYS GLN PHE ARG VAL
SEQRES 20 C 275 ARG ASP GLY GLY HIS ASP TRP GLU TYR TRP HIS SER ALA
SEQRES 21 C 275 LEU TYR GLN CYS LEU PRO PHE VAL THR ARG ILE PHE GLY
SEQRES 22 C 275 LYS GLU
SEQRES 1 D 275 LYS GLN ASN ALA PRO TRP ASN PHE GLN SER LYS VAL VAL
SEQRES 2 D 275 THR ASP THR LEU PHE SER LYS VAL LEU ASN SER LYS ARG
SEQRES 3 D 275 ALA TYR THR VAL PHE LEU PRO LYS SER PHE GLU GLN ASN
SEQRES 4 D 275 LYS GLU LYS LYS TYR PRO VAL LEU TYR LEU LEU HIS GLY
SEQRES 5 D 275 MET TRP GLU THR ASN PRO VAL TRP ALA GLU ARG GLY HIS
SEQRES 6 D 275 VAL LYS ASP VAL MET ASP ARG LEU VAL ALA SER GLY GLU
SEQRES 7 D 275 ALA CYS GLU MET ILE ILE VAL THR PRO ASN ALA GLY GLY
SEQRES 8 D 275 ASN ILE HIS LEU GLU TRP ASN GLY TYR PHE ASP MET PRO
SEQRES 9 D 275 GLY TRP LYS TYR GLU THR PHE PHE TYR THR GLU PHE LEU
SEQRES 10 D 275 PRO TYR ILE GLU LYS LYS TYR ARG VAL ILE GLY ASP ARG
SEQRES 11 D 275 GLN HIS ARG ALA ILE ALA GLY LEU SER MET GLY GLY GLY
SEQRES 12 D 275 GLY ALA THR ASN TYR GLY GLN ARG HIS SER ASP MET PHE
SEQRES 13 D 275 CYS ALA VAL TYR ALA MET SER ALA LEU MET SER ILE PRO
SEQRES 14 D 275 GLU GLN GLY ALA VAL PRO ALA ASP ASP PRO ASN SER LYS
SEQRES 15 D 275 ILE ALA ILE LEU THR ARG SER VAL ILE GLU ASN SER CYS
SEQRES 16 D 275 VAL LYS TYR VAL MET GLU ALA ASP GLU ASP ARG LYS ALA
SEQRES 17 D 275 ASP LEU ARG SER VAL ALA TRP PHE VAL ASP CYS GLY ASP
SEQRES 18 D 275 ASP ASP PHE LEU LEU ASP ARG ASN ILE GLU PHE TYR GLN
SEQRES 19 D 275 ALA MET ARG ASN ALA GLY VAL PRO CYS GLN PHE ARG VAL
SEQRES 20 D 275 ARG ASP GLY GLY HIS ASP TRP GLU TYR TRP HIS SER ALA
SEQRES 21 D 275 LEU TYR GLN CYS LEU PRO PHE VAL THR ARG ILE PHE GLY
SEQRES 22 D 275 LYS GLU
SEQRES 1 E 275 LYS GLN ASN ALA PRO TRP ASN PHE GLN SER LYS VAL VAL
SEQRES 2 E 275 THR ASP THR LEU PHE SER LYS VAL LEU ASN SER LYS ARG
SEQRES 3 E 275 ALA TYR THR VAL PHE LEU PRO LYS SER PHE GLU GLN ASN
SEQRES 4 E 275 LYS GLU LYS LYS TYR PRO VAL LEU TYR LEU LEU HIS GLY
SEQRES 5 E 275 MET TRP GLU THR ASN PRO VAL TRP ALA GLU ARG GLY HIS
SEQRES 6 E 275 VAL LYS ASP VAL MET ASP ARG LEU VAL ALA SER GLY GLU
SEQRES 7 E 275 ALA CYS GLU MET ILE ILE VAL THR PRO ASN ALA GLY GLY
SEQRES 8 E 275 ASN ILE HIS LEU GLU TRP ASN GLY TYR PHE ASP MET PRO
SEQRES 9 E 275 GLY TRP LYS TYR GLU THR PHE PHE TYR THR GLU PHE LEU
SEQRES 10 E 275 PRO TYR ILE GLU LYS LYS TYR ARG VAL ILE GLY ASP ARG
SEQRES 11 E 275 GLN HIS ARG ALA ILE ALA GLY LEU SER MET GLY GLY GLY
SEQRES 12 E 275 GLY ALA THR ASN TYR GLY GLN ARG HIS SER ASP MET PHE
SEQRES 13 E 275 CYS ALA VAL TYR ALA MET SER ALA LEU MET SER ILE PRO
SEQRES 14 E 275 GLU GLN GLY ALA VAL PRO ALA ASP ASP PRO ASN SER LYS
SEQRES 15 E 275 ILE ALA ILE LEU THR ARG SER VAL ILE GLU ASN SER CYS
SEQRES 16 E 275 VAL LYS TYR VAL MET GLU ALA ASP GLU ASP ARG LYS ALA
SEQRES 17 E 275 ASP LEU ARG SER VAL ALA TRP PHE VAL ASP CYS GLY ASP
SEQRES 18 E 275 ASP ASP PHE LEU LEU ASP ARG ASN ILE GLU PHE TYR GLN
SEQRES 19 E 275 ALA MET ARG ASN ALA GLY VAL PRO CYS GLN PHE ARG VAL
SEQRES 20 E 275 ARG ASP GLY GLY HIS ASP TRP GLU TYR TRP HIS SER ALA
SEQRES 21 E 275 LEU TYR GLN CYS LEU PRO PHE VAL THR ARG ILE PHE GLY
SEQRES 22 E 275 LYS GLU
SEQRES 1 F 275 LYS GLN ASN ALA PRO TRP ASN PHE GLN SER LYS VAL VAL
SEQRES 2 F 275 THR ASP THR LEU PHE SER LYS VAL LEU ASN SER LYS ARG
SEQRES 3 F 275 ALA TYR THR VAL PHE LEU PRO LYS SER PHE GLU GLN ASN
SEQRES 4 F 275 LYS GLU LYS LYS TYR PRO VAL LEU TYR LEU LEU HIS GLY
SEQRES 5 F 275 MET TRP GLU THR ASN PRO VAL TRP ALA GLU ARG GLY HIS
SEQRES 6 F 275 VAL LYS ASP VAL MET ASP ARG LEU VAL ALA SER GLY GLU
SEQRES 7 F 275 ALA CYS GLU MET ILE ILE VAL THR PRO ASN ALA GLY GLY
SEQRES 8 F 275 ASN ILE HIS LEU GLU TRP ASN GLY TYR PHE ASP MET PRO
SEQRES 9 F 275 GLY TRP LYS TYR GLU THR PHE PHE TYR THR GLU PHE LEU
SEQRES 10 F 275 PRO TYR ILE GLU LYS LYS TYR ARG VAL ILE GLY ASP ARG
SEQRES 11 F 275 GLN HIS ARG ALA ILE ALA GLY LEU SER MET GLY GLY GLY
SEQRES 12 F 275 GLY ALA THR ASN TYR GLY GLN ARG HIS SER ASP MET PHE
SEQRES 13 F 275 CYS ALA VAL TYR ALA MET SER ALA LEU MET SER ILE PRO
SEQRES 14 F 275 GLU GLN GLY ALA VAL PRO ALA ASP ASP PRO ASN SER LYS
SEQRES 15 F 275 ILE ALA ILE LEU THR ARG SER VAL ILE GLU ASN SER CYS
SEQRES 16 F 275 VAL LYS TYR VAL MET GLU ALA ASP GLU ASP ARG LYS ALA
SEQRES 17 F 275 ASP LEU ARG SER VAL ALA TRP PHE VAL ASP CYS GLY ASP
SEQRES 18 F 275 ASP ASP PHE LEU LEU ASP ARG ASN ILE GLU PHE TYR GLN
SEQRES 19 F 275 ALA MET ARG ASN ALA GLY VAL PRO CYS GLN PHE ARG VAL
SEQRES 20 F 275 ARG ASP GLY GLY HIS ASP TRP GLU TYR TRP HIS SER ALA
SEQRES 21 F 275 LEU TYR GLN CYS LEU PRO PHE VAL THR ARG ILE PHE GLY
SEQRES 22 F 275 LYS GLU
SEQRES 1 G 275 LYS GLN ASN ALA PRO TRP ASN PHE GLN SER LYS VAL VAL
SEQRES 2 G 275 THR ASP THR LEU PHE SER LYS VAL LEU ASN SER LYS ARG
SEQRES 3 G 275 ALA TYR THR VAL PHE LEU PRO LYS SER PHE GLU GLN ASN
SEQRES 4 G 275 LYS GLU LYS LYS TYR PRO VAL LEU TYR LEU LEU HIS GLY
SEQRES 5 G 275 MET TRP GLU THR ASN PRO VAL TRP ALA GLU ARG GLY HIS
SEQRES 6 G 275 VAL LYS ASP VAL MET ASP ARG LEU VAL ALA SER GLY GLU
SEQRES 7 G 275 ALA CYS GLU MET ILE ILE VAL THR PRO ASN ALA GLY GLY
SEQRES 8 G 275 ASN ILE HIS LEU GLU TRP ASN GLY TYR PHE ASP MET PRO
SEQRES 9 G 275 GLY TRP LYS TYR GLU THR PHE PHE TYR THR GLU PHE LEU
SEQRES 10 G 275 PRO TYR ILE GLU LYS LYS TYR ARG VAL ILE GLY ASP ARG
SEQRES 11 G 275 GLN HIS ARG ALA ILE ALA GLY LEU SER MET GLY GLY GLY
SEQRES 12 G 275 GLY ALA THR ASN TYR GLY GLN ARG HIS SER ASP MET PHE
SEQRES 13 G 275 CYS ALA VAL TYR ALA MET SER ALA LEU MET SER ILE PRO
SEQRES 14 G 275 GLU GLN GLY ALA VAL PRO ALA ASP ASP PRO ASN SER LYS
SEQRES 15 G 275 ILE ALA ILE LEU THR ARG SER VAL ILE GLU ASN SER CYS
SEQRES 16 G 275 VAL LYS TYR VAL MET GLU ALA ASP GLU ASP ARG LYS ALA
SEQRES 17 G 275 ASP LEU ARG SER VAL ALA TRP PHE VAL ASP CYS GLY ASP
SEQRES 18 G 275 ASP ASP PHE LEU LEU ASP ARG ASN ILE GLU PHE TYR GLN
SEQRES 19 G 275 ALA MET ARG ASN ALA GLY VAL PRO CYS GLN PHE ARG VAL
SEQRES 20 G 275 ARG ASP GLY GLY HIS ASP TRP GLU TYR TRP HIS SER ALA
SEQRES 21 G 275 LEU TYR GLN CYS LEU PRO PHE VAL THR ARG ILE PHE GLY
SEQRES 22 G 275 LYS GLU
SEQRES 1 H 275 LYS GLN ASN ALA PRO TRP ASN PHE GLN SER LYS VAL VAL
SEQRES 2 H 275 THR ASP THR LEU PHE SER LYS VAL LEU ASN SER LYS ARG
SEQRES 3 H 275 ALA TYR THR VAL PHE LEU PRO LYS SER PHE GLU GLN ASN
SEQRES 4 H 275 LYS GLU LYS LYS TYR PRO VAL LEU TYR LEU LEU HIS GLY
SEQRES 5 H 275 MET TRP GLU THR ASN PRO VAL TRP ALA GLU ARG GLY HIS
SEQRES 6 H 275 VAL LYS ASP VAL MET ASP ARG LEU VAL ALA SER GLY GLU
SEQRES 7 H 275 ALA CYS GLU MET ILE ILE VAL THR PRO ASN ALA GLY GLY
SEQRES 8 H 275 ASN ILE HIS LEU GLU TRP ASN GLY TYR PHE ASP MET PRO
SEQRES 9 H 275 GLY TRP LYS TYR GLU THR PHE PHE TYR THR GLU PHE LEU
SEQRES 10 H 275 PRO TYR ILE GLU LYS LYS TYR ARG VAL ILE GLY ASP ARG
SEQRES 11 H 275 GLN HIS ARG ALA ILE ALA GLY LEU SER MET GLY GLY GLY
SEQRES 12 H 275 GLY ALA THR ASN TYR GLY GLN ARG HIS SER ASP MET PHE
SEQRES 13 H 275 CYS ALA VAL TYR ALA MET SER ALA LEU MET SER ILE PRO
SEQRES 14 H 275 GLU GLN GLY ALA VAL PRO ALA ASP ASP PRO ASN SER LYS
SEQRES 15 H 275 ILE ALA ILE LEU THR ARG SER VAL ILE GLU ASN SER CYS
SEQRES 16 H 275 VAL LYS TYR VAL MET GLU ALA ASP GLU ASP ARG LYS ALA
SEQRES 17 H 275 ASP LEU ARG SER VAL ALA TRP PHE VAL ASP CYS GLY ASP
SEQRES 18 H 275 ASP ASP PHE LEU LEU ASP ARG ASN ILE GLU PHE TYR GLN
SEQRES 19 H 275 ALA MET ARG ASN ALA GLY VAL PRO CYS GLN PHE ARG VAL
SEQRES 20 H 275 ARG ASP GLY GLY HIS ASP TRP GLU TYR TRP HIS SER ALA
SEQRES 21 H 275 LEU TYR GLN CYS LEU PRO PHE VAL THR ARG ILE PHE GLY
SEQRES 22 H 275 LYS GLU
HET CA A 301 1
HET IPA A 302 12
HET IPA A 303 12
HET IPA A 304 12
HET CA B 301 1
HET IPA B 302 12
HET IPA B 303 12
HET IPA B 304 12
HET CA C 301 1
HET IPA C 302 12
HET IPA C 303 12
HET IPA C 304 12
HET CA D 301 1
HET IPA D 302 12
HET IPA D 303 12
HET IPA D 304 12
HET IPA D 305 12
HET CA E 301 1
HET IPA E 302 12
HET CA F 301 1
HET IPA F 302 12
HET IPA F 303 12
HET CA G 301 1
HET IPA G 302 12
HET CA H 301 1
HET IPA H 302 12
HETNAM CA CALCIUM ION
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 9 CA 8(CA 2+)
FORMUL 10 IPA 18(C3 H8 O)
FORMUL 35 HOH *1403(H2 O)
HELIX 1 AA1 PRO A 71 ARG A 76 1 6
HELIX 2 AA2 HIS A 78 SER A 89 1 12
HELIX 3 AA3 TYR A 121 GLU A 128 1 8
HELIX 4 AA4 GLU A 128 TYR A 137 1 10
HELIX 5 AA5 ASP A 142 GLN A 144 5 3
HELIX 6 AA6 SER A 152 HIS A 165 1 14
HELIX 7 AA7 SER A 194 ASN A 206 1 13
HELIX 8 AA8 SER A 207 GLU A 214 1 8
HELIX 9 AA9 ASP A 216 ARG A 224 1 9
HELIX 10 AB1 LEU A 238 ALA A 252 1 15
HELIX 11 AB2 ASP A 266 PHE A 285 1 20
HELIX 12 AB3 PRO B 71 ARG B 76 1 6
HELIX 13 AB4 HIS B 78 GLY B 90 1 13
HELIX 14 AB5 TYR B 121 GLU B 128 1 8
HELIX 15 AB6 GLU B 128 TYR B 137 1 10
HELIX 16 AB7 ASP B 142 GLN B 144 5 3
HELIX 17 AB8 SER B 152 HIS B 165 1 14
HELIX 18 AB9 SER B 194 ASN B 206 1 13
HELIX 19 AC1 SER B 207 GLU B 214 1 8
HELIX 20 AC2 ASP B 216 SER B 225 1 10
HELIX 21 AC3 LEU B 238 ALA B 252 1 15
HELIX 22 AC4 ASP B 266 GLY B 286 1 21
HELIX 23 AC5 PRO C 71 ARG C 76 1 6
HELIX 24 AC6 HIS C 78 SER C 89 1 12
HELIX 25 AC7 TYR C 121 GLU C 128 1 8
HELIX 26 AC8 GLU C 128 TYR C 137 1 10
HELIX 27 AC9 ASP C 142 GLN C 144 5 3
HELIX 28 AD1 SER C 152 HIS C 165 1 14
HELIX 29 AD2 SER C 194 ASN C 206 1 13
HELIX 30 AD3 SER C 207 GLU C 214 1 8
HELIX 31 AD4 ASP C 216 ARG C 224 1 9
HELIX 32 AD5 LEU C 238 ALA C 252 1 15
HELIX 33 AD6 ASP C 266 PHE C 285 1 20
HELIX 34 AD7 PRO D 71 ARG D 76 1 6
HELIX 35 AD8 HIS D 78 SER D 89 1 12
HELIX 36 AD9 TYR D 121 GLU D 128 1 8
HELIX 37 AE1 GLU D 128 TYR D 137 1 10
HELIX 38 AE2 ASP D 142 GLN D 144 5 3
HELIX 39 AE3 SER D 152 HIS D 165 1 14
HELIX 40 AE4 SER D 194 ASN D 206 1 13
HELIX 41 AE5 SER D 207 GLU D 214 1 8
HELIX 42 AE6 ASP D 216 SER D 225 1 10
HELIX 43 AE7 LEU D 238 ALA D 252 1 15
HELIX 44 AE8 ASP D 266 PHE D 285 1 20
HELIX 45 AE9 PRO E 71 ARG E 76 1 6
HELIX 46 AF1 HIS E 78 SER E 89 1 12
HELIX 47 AF2 TYR E 121 GLU E 128 1 8
HELIX 48 AF3 GLU E 128 TYR E 137 1 10
HELIX 49 AF4 ASP E 142 GLN E 144 5 3
HELIX 50 AF5 SER E 152 HIS E 165 1 14
HELIX 51 AF6 SER E 194 ASN E 206 1 13
HELIX 52 AF7 SER E 207 GLU E 214 1 8
HELIX 53 AF8 ASP E 216 ARG E 224 1 9
HELIX 54 AF9 LEU E 238 ALA E 252 1 15
HELIX 55 AG1 ASP E 266 PHE E 285 1 20
HELIX 56 AG2 PRO F 71 ARG F 76 1 6
HELIX 57 AG3 HIS F 78 SER F 89 1 12
HELIX 58 AG4 TYR F 121 GLU F 128 1 8
HELIX 59 AG5 GLU F 128 TYR F 137 1 10
HELIX 60 AG6 ASP F 142 GLN F 144 5 3
HELIX 61 AG7 SER F 152 HIS F 165 1 14
HELIX 62 AG8 SER F 194 ASN F 206 1 13
HELIX 63 AG9 SER F 207 GLU F 214 1 8
HELIX 64 AH1 ASP F 216 ARG F 224 1 9
HELIX 65 AH2 LEU F 238 ALA F 252 1 15
HELIX 66 AH3 ASP F 266 PHE F 285 1 20
HELIX 67 AH4 PRO G 71 ARG G 76 1 6
HELIX 68 AH5 HIS G 78 SER G 89 1 12
HELIX 69 AH6 TYR G 121 GLU G 128 1 8
HELIX 70 AH7 GLU G 128 TYR G 137 1 10
HELIX 71 AH8 ASP G 142 GLN G 144 5 3
HELIX 72 AH9 SER G 152 HIS G 165 1 14
HELIX 73 AI1 SER G 194 ASN G 206 1 13
HELIX 74 AI2 SER G 207 GLU G 214 1 8
HELIX 75 AI3 ASP G 216 SER G 225 1 10
HELIX 76 AI4 LEU G 238 ALA G 252 1 15
HELIX 77 AI5 ASP G 266 PHE G 285 1 20
HELIX 78 AI6 PRO H 71 ARG H 76 1 6
HELIX 79 AI7 HIS H 78 SER H 89 1 12
HELIX 80 AI8 TYR H 121 GLU H 128 1 8
HELIX 81 AI9 GLU H 128 TYR H 137 1 10
HELIX 82 AJ1 ASP H 142 GLN H 144 5 3
HELIX 83 AJ2 SER H 152 HIS H 165 1 14
HELIX 84 AJ3 SER H 194 ASN H 206 1 13
HELIX 85 AJ4 SER H 207 GLU H 214 1 8
HELIX 86 AJ5 ASP H 216 ARG H 224 1 9
HELIX 87 AJ6 LEU H 238 ALA H 252 1 15
HELIX 88 AJ7 ASP H 266 PHE H 285 1 20
SHEET 1 AA1 8 LYS A 24 SER A 32 0
SHEET 2 AA1 8 SER A 37 LEU A 45 -1 O LEU A 45 N LYS A 24
SHEET 3 AA1 8 ILE A 96 PRO A 100 -1 O ILE A 97 N PHE A 44
SHEET 4 AA1 8 VAL A 59 LEU A 63 1 N LEU A 60 O ILE A 96
SHEET 5 AA1 8 ARG A 146 LEU A 151 1 O ALA A 149 N TYR A 61
SHEET 6 AA1 8 ALA A 171 MET A 175 1 O MET A 175 N GLY A 150
SHEET 7 AA1 8 ALA A 227 ASP A 231 1 O PHE A 229 N ALA A 174
SHEET 8 AA1 8 GLN A 257 ARG A 259 1 O GLN A 257 N VAL A 230
SHEET 1 AA2 2 ASP A 115 MET A 116 0
SHEET 2 AA2 2 TRP A 119 LYS A 120 -1 O TRP A 119 N MET A 116
SHEET 1 AA3 8 LYS B 24 SER B 32 0
SHEET 2 AA3 8 SER B 37 LEU B 45 -1 O VAL B 43 N VAL B 26
SHEET 3 AA3 8 ILE B 96 PRO B 100 -1 O ILE B 97 N PHE B 44
SHEET 4 AA3 8 VAL B 59 LEU B 63 1 N LEU B 60 O ILE B 96
SHEET 5 AA3 8 ARG B 146 LEU B 151 1 O ALA B 149 N TYR B 61
SHEET 6 AA3 8 ALA B 171 MET B 175 1 O MET B 175 N GLY B 150
SHEET 7 AA3 8 ALA B 227 ASP B 231 1 O PHE B 229 N ALA B 174
SHEET 8 AA3 8 GLN B 257 ARG B 259 1 O GLN B 257 N VAL B 230
SHEET 1 AA4 2 ASP B 115 MET B 116 0
SHEET 2 AA4 2 TRP B 119 LYS B 120 -1 O TRP B 119 N MET B 116
SHEET 1 AA5 8 LYS C 24 SER C 32 0
SHEET 2 AA5 8 SER C 37 LEU C 45 -1 O LEU C 45 N LYS C 24
SHEET 3 AA5 8 ILE C 96 PRO C 100 -1 O ILE C 97 N PHE C 44
SHEET 4 AA5 8 VAL C 59 LEU C 63 1 N LEU C 60 O ILE C 96
SHEET 5 AA5 8 ARG C 146 LEU C 151 1 O ALA C 149 N LEU C 63
SHEET 6 AA5 8 ALA C 171 MET C 175 1 O MET C 175 N GLY C 150
SHEET 7 AA5 8 ALA C 227 ASP C 231 1 O ALA C 227 N VAL C 172
SHEET 8 AA5 8 GLN C 257 ARG C 259 1 O GLN C 257 N VAL C 230
SHEET 1 AA6 2 ASP C 115 MET C 116 0
SHEET 2 AA6 2 TRP C 119 LYS C 120 -1 O TRP C 119 N MET C 116
SHEET 1 AA7 8 LYS D 24 SER D 32 0
SHEET 2 AA7 8 SER D 37 LEU D 45 -1 O ARG D 39 N LEU D 30
SHEET 3 AA7 8 ILE D 96 PRO D 100 -1 O ILE D 97 N PHE D 44
SHEET 4 AA7 8 VAL D 59 LEU D 63 1 N LEU D 62 O VAL D 98
SHEET 5 AA7 8 ARG D 146 LEU D 151 1 O ALA D 149 N LEU D 63
SHEET 6 AA7 8 ALA D 171 MET D 175 1 O MET D 175 N GLY D 150
SHEET 7 AA7 8 ALA D 227 ASP D 231 1 O PHE D 229 N ALA D 174
SHEET 8 AA7 8 GLN D 257 ARG D 259 1 O GLN D 257 N VAL D 230
SHEET 1 AA8 2 ASP D 115 MET D 116 0
SHEET 2 AA8 2 TRP D 119 LYS D 120 -1 O TRP D 119 N MET D 116
SHEET 1 AA9 8 LYS E 24 SER E 32 0
SHEET 2 AA9 8 SER E 37 LEU E 45 -1 O VAL E 43 N VAL E 26
SHEET 3 AA9 8 ILE E 96 PRO E 100 -1 O ILE E 97 N PHE E 44
SHEET 4 AA9 8 VAL E 59 LEU E 63 1 N LEU E 60 O ILE E 96
SHEET 5 AA9 8 ARG E 146 LEU E 151 1 O ALA E 149 N TYR E 61
SHEET 6 AA9 8 ALA E 171 MET E 175 1 O MET E 175 N GLY E 150
SHEET 7 AA9 8 ALA E 227 ASP E 231 1 O PHE E 229 N ALA E 174
SHEET 8 AA9 8 GLN E 257 ARG E 259 1 O GLN E 257 N VAL E 230
SHEET 1 AB1 2 ASP E 115 MET E 116 0
SHEET 2 AB1 2 TRP E 119 LYS E 120 -1 O TRP E 119 N MET E 116
SHEET 1 AB2 8 LYS F 24 SER F 32 0
SHEET 2 AB2 8 SER F 37 LEU F 45 -1 O LEU F 45 N LYS F 24
SHEET 3 AB2 8 ILE F 96 PRO F 100 -1 O ILE F 97 N PHE F 44
SHEET 4 AB2 8 VAL F 59 LEU F 63 1 N LEU F 60 O ILE F 96
SHEET 5 AB2 8 ARG F 146 LEU F 151 1 O ALA F 149 N TYR F 61
SHEET 6 AB2 8 ALA F 171 MET F 175 1 O MET F 175 N GLY F 150
SHEET 7 AB2 8 ALA F 227 ASP F 231 1 O PHE F 229 N ALA F 174
SHEET 8 AB2 8 GLN F 257 ARG F 259 1 O ARG F 259 N VAL F 230
SHEET 1 AB3 2 ASP F 115 MET F 116 0
SHEET 2 AB3 2 TRP F 119 LYS F 120 -1 O TRP F 119 N MET F 116
SHEET 1 AB4 8 LYS G 24 SER G 32 0
SHEET 2 AB4 8 SER G 37 LEU G 45 -1 O LEU G 45 N LYS G 24
SHEET 3 AB4 8 ILE G 96 PRO G 100 -1 O ILE G 97 N PHE G 44
SHEET 4 AB4 8 VAL G 59 LEU G 63 1 N LEU G 60 O ILE G 96
SHEET 5 AB4 8 ARG G 146 LEU G 151 1 O ALA G 149 N LEU G 63
SHEET 6 AB4 8 ALA G 171 MET G 175 1 O MET G 175 N GLY G 150
SHEET 7 AB4 8 ALA G 227 ASP G 231 1 O PHE G 229 N ALA G 174
SHEET 8 AB4 8 CYS G 256 ARG G 259 1 O GLN G 257 N VAL G 230
SHEET 1 AB5 2 ASP G 115 MET G 116 0
SHEET 2 AB5 2 TRP G 119 LYS G 120 -1 O TRP G 119 N MET G 116
SHEET 1 AB6 8 LYS H 24 SER H 32 0
SHEET 2 AB6 8 SER H 37 LEU H 45 -1 O ARG H 39 N LEU H 30
SHEET 3 AB6 8 ILE H 96 PRO H 100 -1 O ILE H 97 N PHE H 44
SHEET 4 AB6 8 VAL H 59 LEU H 63 1 N LEU H 60 O ILE H 96
SHEET 5 AB6 8 ARG H 146 LEU H 151 1 O ALA H 149 N TYR H 61
SHEET 6 AB6 8 ALA H 171 MET H 175 1 O MET H 175 N GLY H 150
SHEET 7 AB6 8 ALA H 227 ASP H 231 1 O PHE H 229 N ALA H 174
SHEET 8 AB6 8 CYS H 256 ARG H 259 1 O GLN H 257 N VAL H 230
SHEET 1 AB7 2 ASP H 115 MET H 116 0
SHEET 2 AB7 2 TRP H 119 LYS H 120 -1 O TRP H 119 N MET H 116
LINK OD1 ASP A 234 CA CA A 301 1555 1555 2.53
LINK OD2 ASP A 234 CA CA A 301 1555 1555 2.54
LINK OD2 ASP A 235 CA CA A 301 1555 1555 2.61
LINK OE1 GLN A 257 CA CA B 301 1555 1555 2.58
LINK OD1 ASP A 262 CA CA A 301 1555 1555 2.35
LINK OD1 ASP B 234 CA CA B 301 1555 1555 2.56
LINK OD2 ASP B 234 CA CA B 301 1555 1555 2.53
LINK OD2 ASP B 235 CA CA B 301 1555 1555 2.73
LINK OE1 GLN B 257 CA CA A 301 1555 1555 2.47
LINK OD1 ASP B 262 CA CA B 301 1555 1555 2.34
LINK OD1 ASP C 234 CA CA C 301 1555 1555 2.50
LINK OD2 ASP C 234 CA CA C 301 1555 1555 2.44
LINK OD2 ASP C 235 CA CA C 301 1555 1555 2.60
LINK OE1 GLN C 257 CA CA F 301 1555 1555 2.44
LINK OD1 ASP C 262 CA CA C 301 1555 1555 2.34
LINK OD1 ASP D 234 CA CA D 301 1555 1555 2.63
LINK OD2 ASP D 234 CA CA D 301 1555 1555 2.61
LINK OD2 ASP D 235 CA CA D 301 1555 1555 2.59
LINK OE1 GLN D 257 CA CA E 301 1555 1555 2.46
LINK OD1 ASP D 262 CA CA D 301 1555 1555 2.38
LINK OD1 ASP E 234 CA CA E 301 1555 1555 2.53
LINK OD2 ASP E 234 CA CA E 301 1555 1555 2.54
LINK OD2 ASP E 235 CA CA E 301 1555 1555 2.77
LINK OE1 GLN E 257 CA CA D 301 1555 1555 2.56
LINK OD1 ASP E 262 CA CA E 301 1555 1555 2.42
LINK OD1 ASP F 234 CA CA F 301 1555 1555 2.56
LINK OD2 ASP F 234 CA CA F 301 1555 1555 2.51
LINK OD2 ASP F 235 CA CA F 301 1555 1555 2.72
LINK OE1 GLN F 257 CA CA C 301 1555 1555 2.49
LINK OD1 ASP F 262 CA CA F 301 1555 1555 2.34
LINK OD1 ASP G 234 CA CA G 301 1555 1555 2.65
LINK OD2 ASP G 234 CA CA G 301 1555 1555 2.56
LINK OD2 ASP G 235 CA CA G 301 1555 1555 2.81
LINK OE1 GLN G 257 CA CA H 301 1555 1555 2.48
LINK OD1 ASP G 262 CA CA G 301 1555 1555 2.39
LINK OD1 ASP H 234 CA CA H 301 1555 1555 2.62
LINK OD2 ASP H 234 CA CA H 301 1555 1555 2.47
LINK OD2 ASP H 235 CA CA H 301 1555 1555 2.72
LINK OE1 GLN H 257 CA CA G 301 1555 1555 2.45
LINK OD1 ASP H 262 CA CA H 301 1555 1555 2.37
LINK CA CA A 301 O HOH A 554 1555 1555 2.53
LINK CA CA A 301 O HOH A 418 1555 1555 2.56
LINK CA CA B 301 O HOH B 428 1555 1555 2.66
LINK CA CA B 301 O HOH B 521 1555 1555 2.47
LINK CA CA C 301 O HOH C 413 1555 1555 2.63
LINK CA CA C 301 O HOH C 544 1555 1555 2.54
LINK CA CA D 301 O HOH D 558 1555 1555 2.51
LINK CA CA D 301 O HOH D 451 1555 1555 2.53
LINK CA CA E 301 O HOH E 416 1555 1555 2.68
LINK CA CA E 301 O HOH E 522 1555 1555 2.53
LINK CA CA F 301 O HOH F 503 1555 1555 2.49
LINK CA CA F 301 O HOH F 426 1555 1555 2.58
LINK CA CA G 301 O HOH G 440 1555 1555 2.49
LINK CA CA G 301 O HOH G 459 1555 1555 2.44
LINK CA CA H 301 O HOH H 423 1555 1555 2.61
LINK CA CA H 301 O HOH G 518 1555 1555 2.50
SITE 1 AC1 6 ASP A 234 ASP A 235 ASP A 262 HOH A 418
SITE 2 AC1 6 HOH A 554 GLN B 257
SITE 1 AC2 1 ILE A 181
SITE 1 AC3 6 TYR A 126 HIS A 165 ASP A 167 MET A 168
SITE 2 AC3 6 LEU D 108 TRP D 110
SITE 1 AC4 6 GLN A 257 ASP B 234 ASP B 235 ASP B 262
SITE 2 AC4 6 HOH B 428 HOH B 521
SITE 1 AC5 3 MET B 66 ILE B 181 THR B 200
SITE 1 AC6 1 GLU B 122
SITE 1 AC7 6 ASP C 234 ASP C 235 ASP C 262 HOH C 413
SITE 2 AC7 6 HOH C 544 GLN F 257
SITE 1 AC8 2 VAL C 187 THR C 200
SITE 1 AC9 3 ASP C 115 GLU C 122 HIS C 165
SITE 1 AD1 4 MET C 66 GLU C 68 LEU C 151 TRP C 270
SITE 1 AD2 6 ASP D 234 ASP D 235 ASP D 262 HOH D 451
SITE 2 AD2 6 HOH D 558 GLN E 257
SITE 1 AD3 1 HOH D 531
SITE 1 AD4 1 HOH D 517
SITE 1 AD5 2 GLU A 122 ASN D 36
SITE 1 AD6 4 MET D 66 GLU D 68 HIS D 265 TRP D 270
SITE 1 AD7 6 GLN D 257 ASP E 234 ASP E 235 ASP E 262
SITE 2 AD7 6 HOH E 416 HOH E 522
SITE 1 AD8 6 GLN C 257 ASP F 234 ASP F 235 ASP F 262
SITE 2 AD8 6 HOH F 426 HOH F 503
SITE 1 AD9 1 MET F 66
SITE 1 AE1 6 ASP G 234 ASP G 235 ASP G 262 HOH G 440
SITE 2 AE1 6 HOH G 459 GLN H 257
SITE 1 AE2 3 MET G 66 ILE G 181 THR G 200
SITE 1 AE3 6 GLN G 257 HOH G 518 ASP H 234 ASP H 235
SITE 2 AE3 6 ASP H 262 HOH H 423
CRYST1 127.920 135.790 172.590 90.00 90.00 90.00 P 21 21 21 32
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007817 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007364 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005794 0.00000
TER 2114 GLY A 286
TER 4257 GLY B 286
TER 6429 PHE C 285
TER 8568 PHE D 285
TER 10715 PHE E 285
TER 12830 GLY F 286
TER 14928 PHE G 285
TER 17017 PHE H 285
MASTER 611 0 26 88 80 0 30 618479 8 288 176
END |